PHZM_PSEAE
ID PHZM_PSEAE Reviewed; 334 AA.
AC Q9HWH2;
DT 27-SEP-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Phenazine-1-carboxylate N-methyltransferase {ECO:0000305};
DE EC=2.1.1.327 {ECO:0000269|PubMed:17253782};
GN Name=phzM {ECO:0000303|PubMed:16946471};
GN OrderedLocusNames=PA4209 {ECO:0000312|EMBL:AAG07596.1};
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
RN [2]
RP CRYSTALLIZATION, AND SUBUNIT.
RX PubMed=16946471; DOI=10.1107/s1744309106029149;
RA Gohain N., Thomashow L.S., Mavrodi D.V., Blankenfeldt W.;
RT "The purification, crystallization and preliminary structural
RT characterization of PhzM, a phenazine-modifying methyltransferase from
RT Pseudomonas aeruginosa.";
RL Acta Crystallogr. F 62:887-890(2006).
RN [3] {ECO:0007744|PDB:2IP2}
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS), FUNCTION, CATALYTIC ACTIVITY,
RP ACTIVITY REGULATION, PATHWAY, SUBUNIT, AND DOMAIN.
RX PubMed=17253782; DOI=10.1021/bi6024403;
RA Parsons J.F., Greenhagen B.T., Shi K., Calabrese K., Robinson H.,
RA Ladner J.E.;
RT "Structural and functional analysis of the pyocyanin biosynthetic protein
RT PhzM from Pseudomonas aeruginosa.";
RL Biochemistry 46:1821-1828(2007).
CC -!- FUNCTION: Involved in the biosynthesis of pyocyanine, a blue-pigmented
CC phenazine derivative, which plays a role in virulence. Converts
CC phenazine-1-carboxylate (PCA) to 5-methylphenazine-1-carboxylate (5-
CC methyl-PCA). {ECO:0000269|PubMed:17253782}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=phenazine-1-carboxylate + S-adenosyl-L-methionine = 5-methyl-
CC phenazine-1-carboxylate + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:49112, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:62221, ChEBI:CHEBI:62248; EC=2.1.1.327;
CC Evidence={ECO:0000269|PubMed:17253782};
CC -!- ACTIVITY REGULATION: In vitro, requires PhzS for activity.
CC {ECO:0000269|PubMed:17253782}.
CC -!- PATHWAY: Secondary metabolite biosynthesis; pyocyanine biosynthesis.
CC {ECO:0000269|PubMed:17253782}.
CC -!- SUBUNIT: Homodimer in solution (PubMed:16946471, PubMed:17253782).
CC Probably interacts transiently with PhzS (PubMed:17253782).
CC {ECO:0000269|PubMed:16946471, ECO:0000269|PubMed:17253782}.
CC -!- DOMAIN: Contains an N-terminal dimerization domain. The C-terminal
CC region contains the S-adenosyl-L-methionine binding site.
CC {ECO:0000269|PubMed:17253782}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. Cation-independent O-methyltransferase family.
CC {ECO:0000255|PROSITE-ProRule:PRU01020}.
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DR EMBL; AE004091; AAG07596.1; -; Genomic_DNA.
DR PIR; F83120; F83120.
DR RefSeq; NP_252898.1; NC_002516.2.
DR RefSeq; WP_003093617.1; NZ_QZGE01000013.1.
DR PDB; 2IP2; X-ray; 1.80 A; A/B=1-334.
DR PDBsum; 2IP2; -.
DR AlphaFoldDB; Q9HWH2; -.
DR SMR; Q9HWH2; -.
DR STRING; 287.DR97_3702; -.
DR PaxDb; Q9HWH2; -.
DR PRIDE; Q9HWH2; -.
DR DNASU; 880514; -.
DR EnsemblBacteria; AAG07596; AAG07596; PA4209.
DR GeneID; 880514; -.
DR KEGG; pae:PA4209; -.
DR PATRIC; fig|208964.12.peg.4409; -.
DR PseudoCAP; PA4209; -.
DR HOGENOM; CLU_005533_12_0_6; -.
DR InParanoid; Q9HWH2; -.
DR OMA; CTEPWTW; -.
DR PhylomeDB; Q9HWH2; -.
DR BioCyc; MetaCyc:MON-16021; -.
DR BioCyc; PAER208964:G1FZ6-4282-MON; -.
DR BRENDA; 2.1.1.327; 5087.
DR UniPathway; UPA00235; -.
DR EvolutionaryTrace; Q9HWH2; -.
DR PHI-base; PHI:7390; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0102168; F:5-methyl-phenazine-1-carboxylate N-methyltransferase activity; IEA:RHEA.
DR GO; GO:0008171; F:O-methyltransferase activity; IEA:InterPro.
DR GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IDA:PseudoCAP.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR031725; ASMT_dimerisation.
DR InterPro; IPR016461; COMT-like.
DR InterPro; IPR001077; O_MeTrfase_dom.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR Pfam; PF16864; Dimerisation2; 1.
DR Pfam; PF00891; Methyltransf_2; 1.
DR PIRSF; PIRSF005739; O-mtase; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR PROSITE; PS51683; SAM_OMT_II; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Methyltransferase; Reference proteome;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..334
FT /note="Phenazine-1-carboxylate N-methyltransferase"
FT /id="PRO_0000441707"
FT BINDING 198
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT BINDING 241
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT HELIX 6..30
FT /evidence="ECO:0007829|PDB:2IP2"
FT HELIX 33..38
FT /evidence="ECO:0007829|PDB:2IP2"
FT HELIX 44..51
FT /evidence="ECO:0007829|PDB:2IP2"
FT HELIX 55..67
FT /evidence="ECO:0007829|PDB:2IP2"
FT STRAND 70..74
FT /evidence="ECO:0007829|PDB:2IP2"
FT TURN 75..77
FT /evidence="ECO:0007829|PDB:2IP2"
FT STRAND 78..81
FT /evidence="ECO:0007829|PDB:2IP2"
FT HELIX 83..86
FT /evidence="ECO:0007829|PDB:2IP2"
FT STRAND 89..91
FT /evidence="ECO:0007829|PDB:2IP2"
FT HELIX 96..102
FT /evidence="ECO:0007829|PDB:2IP2"
FT HELIX 105..109
FT /evidence="ECO:0007829|PDB:2IP2"
FT TURN 110..112
FT /evidence="ECO:0007829|PDB:2IP2"
FT HELIX 113..119
FT /evidence="ECO:0007829|PDB:2IP2"
FT HELIX 123..128
FT /evidence="ECO:0007829|PDB:2IP2"
FT HELIX 132..138
FT /evidence="ECO:0007829|PDB:2IP2"
FT HELIX 140..150
FT /evidence="ECO:0007829|PDB:2IP2"
FT HELIX 151..153
FT /evidence="ECO:0007829|PDB:2IP2"
FT HELIX 154..163
FT /evidence="ECO:0007829|PDB:2IP2"
FT STRAND 170..174
FT /evidence="ECO:0007829|PDB:2IP2"
FT HELIX 180..188
FT /evidence="ECO:0007829|PDB:2IP2"
FT STRAND 193..198
FT /evidence="ECO:0007829|PDB:2IP2"
FT HELIX 204..209
FT /evidence="ECO:0007829|PDB:2IP2"
FT HELIX 211..215
FT /evidence="ECO:0007829|PDB:2IP2"
FT STRAND 218..224
FT /evidence="ECO:0007829|PDB:2IP2"
FT TURN 226..228
FT /evidence="ECO:0007829|PDB:2IP2"
FT STRAND 235..241
FT /evidence="ECO:0007829|PDB:2IP2"
FT HELIX 243..245
FT /evidence="ECO:0007829|PDB:2IP2"
FT HELIX 248..261
FT /evidence="ECO:0007829|PDB:2IP2"
FT STRAND 267..272
FT /evidence="ECO:0007829|PDB:2IP2"
FT STRAND 277..279
FT /evidence="ECO:0007829|PDB:2IP2"
FT HELIX 282..295
FT /evidence="ECO:0007829|PDB:2IP2"
FT HELIX 302..311
FT /evidence="ECO:0007829|PDB:2IP2"
FT STRAND 314..322
FT /evidence="ECO:0007829|PDB:2IP2"
FT TURN 323..325
FT /evidence="ECO:0007829|PDB:2IP2"
FT STRAND 326..333
FT /evidence="ECO:0007829|PDB:2IP2"
SQ SEQUENCE 334 AA; 36357 MW; 27D9717ECA12A1B5 CRC64;
MNNSNLAAAR NLIQVVTGEW KSRCVYVATR LGLADLIESG IDSDETLAAA VGSDAERIHR
LMRLLVAFEI FQGDTRDGYA NTPTSHLLRD VEGSFRDMVL FYGEEFHAAW TPACEALLSG
TPGFELAFGE DFYSYLKRCP DAGRRFLLAM KASNLAFHEI PRLLDFRGRS FVDVGGGSGE
LTKAILQAEP SARGVMLDRE GSLGVARDNL SSLLAGERVS LVGGDMLQEV PSNGDIYLLS
RIIGDLDEAA SLRLLGNCRE AMAGDGRVVV IERTISASEP SPMSVLWDVH LFMACAGRHR
TTEEVVDLLG RGGFAVERIV DLPMETRMIV AARA
